ID   C135A_MYCTO             Reviewed;         449 AA.
AC   P9WPN0; L0T6C2; O08447;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Putative cytochrome P450 135A1;
DE            EC=1.14.-.-;
GN   Name=cyp135A1; OrderedLocusNames=MT0342;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK44565.1; -; Genomic_DNA.
DR   PIR; H70526; H70526.
DR   RefSeq; WP_003401650.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPN0; -.
DR   SMR; P9WPN0; -.
DR   EnsemblBacteria; AAK44565; AAK44565; MT0342.
DR   GeneID; 45424294; -.
DR   KEGG; mtc:MT0342; -.
DR   PATRIC; fig|83331.31.peg.362; -.
DR   HOGENOM; CLU_001570_5_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..449
FT                   /note="Putative cytochrome P450 135A1"
FT                   /id="PRO_0000426923"
FT   BINDING         383
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   449 AA;  50011 MW;  192E3CF1855EDCF5 CRC64;
     MASTLTTGLP PGPRLPRYLQ SVLYLRFREW FLPAMHRKYG DVFSLRVPPY ADNLVVYTRP
     EHIKEIFAAD PRSLHAGEGN HILGFVMGEH SVLMTDEAEH ARMRSLLMPA FTRAALRGYR
     DMIASVAREH ITRWRPHATI NSLDHMNALT LDIILRVVFG VTDPKVKAEL TSRLQQIINI
     HPAILAGVPY PSLKRMNPWK RFFHNQTKID EILYREIASR RIDSDLTART DVLSRLLQTK
     DTPTKPLTDA ELRDQLITLL LAGHETTAAA LSWTLWELAH APEIQSQVVW AAVGGDDGFL
     EAVLKEGMRR HTVIASTARK VTAPAEIGGW RLPAGTVVNT SILLAHASEV SHPKPTEFRP
     SRFLDGSVAP NTWLPFGGGV RRCLGFGFAL TEGAVILQEI FRRFTITAAG PSKGETPLVR
     NITTVPKHGA HLRLIPQRRL GGLGDSDPP